Crystal structure of the YffB protein from Pseudomonas aeruginosa suggests a glutathione-dependent thiol reductase function View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2004-12

AUTHORS

Alexey Teplyakov, Sadhana Pullalarevu, Galina Obmolova, Victoria Doseeva, Andrey Galkin, Osnat Herzberg, Miroslawa Dauter, Zbigniew Dauter, Gary L Gilliland

ABSTRACT

BACKGROUND: The yffB (PA3664) gene of Pseudomonas aeruginosa encodes an uncharacterized protein of 13 kDa molecular weight with a marginal sequence similarity to arsenate reductase from Escherichia coli. The crystal structure determination of YffB was undertaken as part of a structural genomics effort in order to assist with the functional assignment of the protein. RESULTS: The structure was determined at 1.0 A resolution by single-wavelength anomalous diffraction. The fold is very similar to that of arsenate reductase, which is an extension of the thioredoxin fold. CONCLUSION: Given the conservation of the functionally important residues and the ability to bind glutathione, YffB is likely to function as a GSH-dependent thiol reductase. More... »

PAGES

5

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Identifiers

URI

http://scigraph.springernature.com/pub.10.1186/1472-6807-4-5

DOI

http://dx.doi.org/10.1186/1472-6807-4-5

DIMENSIONS

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PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/15102337


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